PMID: 6275379Jan 1, 1982

Characterization of pro-opiocortin-converting activity in purified secretory granules from rat pituitary neurointermediate lobe

Proceedings of the National Academy of Sciences of the United States of America
Y P Loh, H Gainer

Abstract

Lysates of secretory granules from rat pituitary neurointermediate lobes were incubated with [3H]arginine- or [3H]phenylalanine-labeled toad pro-opiocortin. The processed products formed were identified by immunoprecipitation with adrenocorticotropin (ACTH) and endorphin antisera and by migration behavior on acid/urea/polyacrylamide gels. Pro-opiocortin was cleaved by the proteolytic activity in the secretory granule fraction to approximately 21,000 Mr ACTH, approximately 13,000 Mr ACTH, alpha-melanotropin, 16,000 Mr NH2-terminal glycopeptide, beta-lipotropin, and an endorphin-related peptide. Characterization of this pro-opiocortin-converting activity shows that it (i) is present in membrane and soluble fractions of the granule lysates, (ii) has a pH optimum of 5.0, (iii) appears to cleave at pairs of basic amino acid residues in the precursor, and (iv) is inhibited by leupeptin, pepstatin A, and p-chloromercuribenzoate but not diisopropyl fluorophosphate, N alpha-p-tosyl-L-lysine chloromethyl ketone hydrochloride, chloroquine, or EDTA. These inhibitor studies suggest that the converting-enzyme activity is due to an acid thiol, arginyl protease, distinct from any known cathepsin B-like activity.

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May 1, 1982·Peptides·T L O'Donohue, D M Dorsa
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Aug 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·K DochertyD F Steiner
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Related Concepts

Corticotropin
Cytoplasmic Granules
Melanocyte stimulating hormone
Endopeptidases
Pituitary Stalk
Pituitary Hormones, Anterior
Opiocortin
Protease Inhibitors
Protein Precursors
Subtilisin-Like Proprotein Convertases

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